Modifying the Microenvironment of Epoxy Resin to Improve the Activity of Immobilized 7α-Hydroxysteroid Dehydrogenases.
7α-Hydroxysteroid dehydrogenases
Epoxy resin
Immobilization
Microenvironment
Modification
Journal
Applied biochemistry and biotechnology
ISSN: 1559-0291
Titre abrégé: Appl Biochem Biotechnol
Pays: United States
ID NLM: 8208561
Informations de publication
Date de publication:
Apr 2021
Apr 2021
Historique:
received:
29
06
2020
accepted:
09
11
2020
pubmed:
24
11
2020
medline:
7
7
2021
entrez:
23
11
2020
Statut:
ppublish
Résumé
7α-Hydroxysteroid dehydrogenase (7α-HSDH) is one of the key enzymes in the catalytic reaction of taurochenodeoxycholic acid (TCDCA). To improve the activity of immobilized 7α-HSDH, the microenvironment of immobilized 7α-HSDH was modified with epoxy resin and ethanediamine (EDA). The amino-epoxy support was characterized by Fourier transform infrared (FTIR), Spectrometer elemental analysis (EA), scanning electron microscopy (SEM), contact angle (CA), and Zetasizer. The effects of the immobilization of 7α-HSDH on the amino-epoxy resin and epoxy resin were studied. The results indicated that the relative activity of immobilized 7α-HSDH on the amino-epoxy resin increased by approximately 80%. Meanwhile, the immobilized 7α-HSDH showed favorable thermal stability and operational stability. The thermal stability of immobilized 7α-HSDH increased at temperatures ranging from 15 to 35 °C, while the relative activities of 7α-HSDH immobilized on the amino-epoxy resin and epoxy resin retained 56.4% and 61.0%. After 6 cycles, the residual activities of the 7α-HSDH immobilized on the amino-epoxy resin and epoxy resin were 81.4% and 89.5%, respectively.
Identifiants
pubmed: 33225381
doi: 10.1007/s12010-020-03473-w
pii: 10.1007/s12010-020-03473-w
doi:
Substances chimiques
Enzymes, Immobilized
0
Epoxy Resins
0
Hydroxysteroid Dehydrogenases
EC 1.1.-
7 alpha-hydroxysteroid dehydrogenase
EC 1.1.1.159
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
925-939Subventions
Organisme : The National Science and Technology Major Projects for "Major New Drugs Innovation and Development"
ID : 2017ZX09301306-007
Organisme : The Scientific and Technological Research Program of Chongqing Municipal Education Commission
ID : KJQN202001427;KJ1601216
Références
Bakonyi, D., & Hummel, W. (2017). Cloning, expression, and biochemical characterization of a novel NADP+-dependent 7α-hydroxysteroid dehydrogenase from Clostridium difficile and its application for the oxidation of bile acids. Enzyme and Microbial Technology, 99, 16–24.
pubmed: 28193327
Barbosa, O., Torres, R., Ortiz, C., Berenguer-Murcia, Á., Rodrigues, R. C., & Fernandez-Lafuente, R. (2013). Heterofunctional supports in enzyme immobilization: from traditional immobilization protocols to opportunities in tuning enzyme properties. Biomacromolecules, 14(8), 2433–2462.
pubmed: 23822160
Barbosa, O., Ortiz, C., Berenguer-Murcia, A., Torres, R., Rodrigues, R. C., & Fernandez-Lafuente, R. (2015). Strategies for the one-step immobilization-purification of enzymes as industrial biocatalysts. Biotechnology Advances, 33(5), 435–456.
pubmed: 25777494
Barsbay, M., Güven, O., & Kodama, Y. (2016). Amine functionalization of cellulose surface grafted with glycidyl methacrylate by γ-initiated RAFT polymerization. Radiation Physics and Chemistry, 124, 140–144.
Bayramoglu, G., Altintas, B., Yilmaz, M., & Arica, M. Y. (2011). Immobilization of chloroperoxidase onto highly hydrophilic polyethylene chains via bio-conjugation: catalytic properties and stabilities. Bioresource Technology, 102(2), 475–482.
pubmed: 20829037
Bilal, M., Rasheed, T., Zhao, Y., Iqbal, H. M. N., & Cui, J. (2018). “Smart” chemistry and its application in peroxidase immobilization using different support materials. International Journal of Biological Macromolecules, 119, 278–290.
pubmed: 30041033
Bilal, M., Cui, J., & Iqbal, H. M. N. (2019). Tailoring enzyme microenvironment: state-of-the-art strategy to fulfill the quest for efficient bio-catalysis. International Journal of Biological Macromolecules, 130, 186–196.
pubmed: 30817963
Bolivar, J. M., & Nidetzky, B. (2019). The microenvironment in immobilized enzymes: methods of characterization and its role in determining enzyme performance. Molecules, 24, 3460.
pmcid: 6803829
Bornscheuer, U. T. (2003). Immobilizing enzymes: how to create more suitable biocatalysts. Angewandte Chemie (International Ed. in English), 42(29), 3336–3337.
Chen, C. S., Bulkin, B. J., & Pearce, E. M. (1982). New epoxy resins. II. The preparation, characterization, and curing of epoxy resins and their copolymers. Journal of Applied Polymer Science, 27(9), 3289–3312.
Cui, J., & Jia, S. (2017). Organic–inorganic hybrid nanoflowers: a novel host platform for immobilizing biomolecules. Coordination Chemistry Reviews, 352, 249–263.
Deshuai, L., Bochu, W., Jun, T., & Liancai, Z. (2014). Carboxyl-terminal and Arg38 are essential for activity of the 7α-hydroxysteroid dehydrogenase from Clostridium absonum. Protein & Peptide Letters, 21(9):894–900
Donia, A., Atia, A., & Abouzayed, F. (2012). Preparation and characterization of nano-magnetic cellulose with fast kinetic properties towards the adsorption of some metal ions. Chemical Engineering Journal, 191, 22–30.
Duan, Z., He, H., Liang, W., Wang, Z., He, L., & Zhang, X. (2018). Tensile, quasistatic and dynamic fracture properties of nano-Al2O3-modified epoxy resin. Materials, 11(6), 905.
pmcid: 6025226
Engel, S., Hock, H., Bocola, M., Keul, H., Schwaneberg, U., & Moller, M. (2016). CaLB catalyzed conversion of epsilon-caprolactone in aqueous medium. Part 1: immobilization of CaLB to microgels. Polymers, 8, 16.
Ferrandi, E. E., Bertolesi, G. M., Polentini, F., Negri, A., Riva, S., & Monti, D. (2012). In search of sustainable chemical processes: cloning, recombinant expression, and functional characterization of the 7α-and 7β-hydroxysteroid dehydrogenases from Clostridium absonum. Applied Microbiology and Biotechnology, 95(5), 1221–1233.
pubmed: 22198717
Gao, B., Wang, X., & Shen, Y. (2006). Studies on characters of immobilizing penicillin G acylase on a novel composite support PEI/SiO 2. Biochemical Engineering Journal, 28(2), 140–147.
He, X. Y., Merz, G., Mehta, P., Schulz, H., & Yang, S. Y. (1999). Human brain short chain L-3-hydroxyacyl coenzyme A dehydrogenase is a single-domain multifunctional enzyme. Characterization of a novel 17beta-hydroxysteroid dehydrogenase. Journal of Biological Chemistry, 274(21), 15014–15019.
Hildebrand, F., & Lütz, S. (2006). Immobilisation of alcohol dehydrogenase from Lactobacillus brevis and its application in a plug-flow reactor. Tetrahedron: Asymmetry, 17(23), 3219–3225.
Ji, Q., Tan, J., Zhu, L., Lou, D., & Wang, B. (2016). Preparing tauroursodeoxycholic acid (TUDCA) using a double-enzyme-coupled system. Biochemical Engineering Journal, 105, 1–9.
Jin, F. L., Li, X., & Park, S. J. (2015). Synthesis and application of epoxy resins: a review. Journal of Industrial and Engineering Chemistry, 29, 1–11.
Klotzbach, T. L., Watt, M., Ansari, Y., & Minteer, S. D. (2008). Improving the microenvironment for enzyme immobilization at electrodes by hydrophobically modifying chitosan and Nafion (R) polymers. Journal of Membrane Science, 311(1-2), 81–88.
Liu, C.-H., Lin, Y.-H., Chen, C.-Y., & Chang, J.-S. (2009). Characterization of Burkholderia lipase immobilized on celite carriers. Journal of the Taiwan Institute of Chemical Engineers, 40(4), 359–363.
Liu, K., Li, X.-f., Li, X.-m., He, B.-h., & Zhao, G.-l. (2010). Lowering the cationic demand caused by PGA in papermaking by solute adsorption and immobilized pectinase on chitosan beads. Carbohydrate Polymers, 82(3), 648–652.
Liu, J., Bai, S., Jin, Q., Zhong, H., Li, C., & Yang, Q. (2012). Improved catalytic performance of lipase accommodated in the mesoporous silicas with polymer-modified microenvironment. Langmuir, 28(25), 9788–9796.
pubmed: 22642540
Liu, J., Peng, J., Shen, S., Jin, Q., Li, C., & Yang, Q. (2013). Enzyme entrapped in polymer-modified nanopores: the effects of macromolecular crowding and surface hydrophobicity. Chemistry--A European Journal, 19(8), 2711–2719.
Lou, D., Wang, B., Tan, J., Zhu, L., Cen, X., Ji, Q., & Wang, Y. (2016). The three-dimensional structure of Clostridium absonum 7α-hydroxysteroid dehydrogenase: new insights into the conserved arginines for NADP (H) recognition. Scientific Reports, 6(1), 22885.
pubmed: 26961171
pmcid: 4785404
Ma, H., Zhang, X., Ju, F., & Tsai, S. B. (2018). A study on curing kinetics of nano-phase modified epoxy resin. Scientific Reports, 8(1), 3045.
pubmed: 29445228
pmcid: 5813017
Manoel, E. A., Santos, J. C. S. D., Freire, D. M. G., Rueda, N., & Fernandez-Lafuente, R. (2015). Immobilization of lipases on hydrophobic supports involves the open form of the enzyme. Enzyme and Microbial Technology, 71, 53–57.
pubmed: 25765310
Mateo, C., Grazú, V., Pessela, B., Montes, T., Palomo, J., Torres, R., López-Gallego, F., Fernández-Lafuente, R., & Guisán, J. (2007). Advances in the design of new epoxy supports for enzyme immobilization–stabilization. Biochemical Society Transactions, 35(6), 1593–1601.
pubmed: 18031273
Mateo, C., Grazu, V., Palomo, J. M., Lopez-Gallego, F., Fernandez-Lafuente, R., & Guisan, J. M. (2007). Immobilization of enzymes on heterofunctional epoxy supports. Nature Protocols, 2(5), 1022–1033.
pubmed: 17546007
Mateo, C., Palomo, J. M., Fernandez-Lorente, G., Guisan, J. M., & Fernandez-Lafuente, R. (2007). Improvement of enzyme activity, stability and selectivity via immobilization techniques. Enzyme and Microbial Technology, 40(6), 1451–1463.
Moeller, G., & Adamski, J. (2009). Integrated view on 17beta-hydroxysteroid dehydrogenases. Molecular and Cellular Endocrinology, 301(1-2), 7–19.
pubmed: 19027824
Palomo, J. M., Munoz, G., Fernandezlorente, G., Mateo, C., & Fernandezlafuente, R. (2002). Interfacial adsorption of lipases on very hydrophobic support (Octadecyl-Sepabeads): immobilization, hyperactivation and stabilization of the open form of lipases. Journal of Molecular Catalysis B: Enzymatic, 19, 279–286.
Peters, G. H., Svendsen, A., Langberg, H., Vind, J., Patkar, S. A., Toxvaerd, S., & Kinnunen, P. K. (1998). Active serine involved in the stabilization of the active site loop in the Humicola lanuginosa lipase. Biochemistry, 37(36), 12375–12383.
pubmed: 9730809
PragyanMohan. (2013). A critical review: the modification, properties, and applications of epoxy resins. Journal of Macromolecular Science: Part D - Reviews in Polymer Processing, 52, 107–125.
Ren, S., Li, C., Jiao, X., Jia, S., Jiang, Y., Bilal, M., & Cui, J. (2019). Recent progress in multienzymes co-immobilization and multienzyme system applications. Chemical Engineering Journal, 373, 1254–1278.
Sánchez, A., Cruz, J., Rueda, N., Santos, J. C. S. D., Torres, R., Ortiz, C., Villalonga, R., & Lafuente, R. F. (2016). Inactivation of immobilized trypsin under dissimilar conditions produces trypsin molecules with different structures. RSC Advances, 6(33), 27329–27334.
Stepankova, V., Bidmanova, S., Koudelakova, T., Prokop, Z., Chaloupkova, R., & Damborsky, J. (2013). Strategies for stabilization of enzymes in organic solvents. ACS Catalysis, 3(12), 2823–2836.
Talbert, J. N., & Goddard, J. M. (2012). Enzymes on material surfaces. Colloids and Surfaces B: Biointerfaces, 93, 8–19.
pubmed: 22269888
Tang, C. Y., Kwon, Y. N., & Leckie, J. O. (2009). Effect of membrane chemistry and coating layer on physiochemical properties of thin film composite polyamide RO and NF membranes : I. FTIR and XPS characterization of polyamide and coating layer chemistry. Desalination, 242, 149–167.
Torres, R., Mateo, C., Fernández-Lorente, G., Ortiz, C., Fuentes, M., Palomo, J. M., Guisan, J. M., & Fernández-Lafuente, R. (2003). A novel heterofunctional epoxy-amino sepabeads for a new enzyme immobilization protocol: immobilization-stabilization of β-galactosidase from Aspergillus oryzae. Biotechnology Progress, 19(3), 1056–1060.
pubmed: 12790680
Wu, X., Hou, M., & Ge, J. (2015). Metal-organic frameworks and inorganic nanoflowers: a type of emerging inorganic crystal nanocarriers for enzyme immobilization. Catalysis Science & Technology, 5(12), 5077–5085. https://doi.org/10.1039/C5CY01181G .
doi: 10.1039/C5CY01181G
Yang, G., Wu, J., Xu, G., & Yang, L. (2009). Enhancement of the activity and enantioselectivity of lipase in organic systems by immobilization onto low-cost support. Journal of Molecular Catalysis B: Enzymatic, 57(1-4), 96–103.
Yang, Q., Wang, B., Zhang, Z., Lou, D., Tan, J., & Zhu, L. (2017). The effects of macromolecular crowding and surface charge on the properties of an immobilized enzyme: activity, thermal stability, catalytic efficiency and reusability. RSC Advances, 7(60), 38028–38036.